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PDBsum entry 2rf9

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Top Page protein Protein-protein interface(s) links
Transferase PDB id
2rf9
Jmol
Contents
Protein chains
280 a.a.
27 a.a.
26 a.a.
HEADER    TRANSFERASE                             28-SEP-07   2RF9
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE EGFR KINASE
TITLE    2 DOMAIN AND A MIG6 PEPTIDE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: PROTEIN KINASE DOMAIN;
COMPND   5 SYNONYM: RECEPTOR TYROSINE-PROTEIN KINASE ERBB-1;
COMPND   6 EC: 2.7.10.1;
COMPND   7 ENGINEERED: YES;
COMPND   8 MOL_ID: 2;
COMPND   9 MOLECULE: ERBB RECEPTOR FEEDBACK INHIBITOR 1;
COMPND  10 CHAIN: C, D;
COMPND  11 FRAGMENT: SEQUENCE DATABASE RESIDUES, 315-374;
COMPND  12 SYNONYM: MITOGEN-INDUCIBLE GENE 6 PROTEIN, MIG-6;
COMPND  13 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: EGFR, ERBB1;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULORVIRUS;
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC-HT;
SOURCE  12 MOL_ID: 2;
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  14 ORGANISM_COMMON: HUMAN;
SOURCE  15 ORGANISM_TAXID: 9606;
SOURCE  16 GENE: ERRFI1, MIG6;
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  21 EXPRESSION_SYSTEM_PLASMID: PGEX6P1
KEYWDS    KINASE DOMAIN, INHIBITION, DIMER, PEPTIDE, ALTERNATIVE
KEYWDS   2 SPLICING, ANTI-ONCOGENE, ATP-BINDING, CELL CYCLE, DISEASE
KEYWDS   3 MUTATION, GLYCOPROTEIN, MEMBRANE, NUCLEOTIDE-BINDING,
KEYWDS   4 PHOSPHORYLATION, POLYMORPHISM, RECEPTOR, SECRETED,
KEYWDS   5 TRANSFERASE, TRANSMEMBRANE, TYROSINE-PROTEIN KINASE, UBL
KEYWDS   6 CONJUGATION, CYTOPLASM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    X.ZHANG,K.A.PICKIN,R.BOSE,N.JURA,P.A.COLE,J.KURIYAN
REVDAT   2   24-FEB-09 2RF9    1       VERSN
REVDAT   1   04-DEC-07 2RF9    0
JRNL        AUTH   X.ZHANG,K.A.PICKIN,R.BOSE,N.JURA,P.A.COLE,J.KURIYAN
JRNL        TITL   INHIBITION OF THE EGF RECEPTOR BY BINDING OF MIG6
JRNL        TITL 2 TO AN ACTIVATING KINASE DOMAIN INTERFACE.
JRNL        REF    NATURE                        V. 450   741 2007
JRNL        REFN                   ISSN 0028-0836
JRNL        PMID   18046415
JRNL        DOI    10.1038/NATURE05998
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.11
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 84.5
REMARK   3   NUMBER OF REFLECTIONS             : 8319
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.272
REMARK   3   FREE R VALUE                     : 0.329
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.600
REMARK   3   FREE R VALUE TEST SET COUNT      : 455
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4435
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 68.35
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -24.63500
REMARK   3    B22 (A**2) : 0.86500
REMARK   3    B33 (A**2) : 23.77100
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -16.14000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.176 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.107 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.449 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.400 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : 67.05
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2RF9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-OCT-07.
REMARK 100 THE RCSB ID CODE IS RCSB044786.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 07-JUN-06
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ALS
REMARK 200  BEAMLINE                       : 8.2.1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9081
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.8
REMARK 200  DATA REDUNDANCY                : 3.300
REMARK 200  R MERGE                    (I) : 0.14700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 6.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.63
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.3
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20
REMARK 200  R MERGE FOR SHELL          (I) : 0.41000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2GS7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 300 MM KAC, 10%
REMARK 280  GLYCEROL AND 100 MM NAAC, PH 5.0, VAPOR DIFFUSION, HANGING
REMARK 280  DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y,-Z
REMARK 290       3555   X+1/2,Y+1/2,Z
REMARK 290       4555   -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       94.38100
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       21.32500
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       94.38100
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       21.32500
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1840 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1800 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   669
REMARK 465     ALA A   670
REMARK 465     MET A   671
REMARK 465     GLY A   672
REMARK 465     GLU A   673
REMARK 465     ALA A   674
REMARK 465     ALA A   726
REMARK 465     THR A   727
REMARK 465     SER A   728
REMARK 465     GLU A   848
REMARK 465     GLY A   849
REMARK 465     ASP A   960
REMARK 465     GLU A   961
REMARK 465     ARG A   962
REMARK 465     MET A   963
REMARK 465     HIS A   964
REMARK 465     LEU A   965
REMARK 465     PRO A   966
REMARK 465     SER A   967
REMARK 465     PRO A   968
REMARK 465     THR A   969
REMARK 465     ASP A   970
REMARK 465     SER A   971
REMARK 465     ASN A   972
REMARK 465     PHE A   973
REMARK 465     TYR A   974
REMARK 465     ARG A   975
REMARK 465     ALA A   976
REMARK 465     LEU A   977
REMARK 465     MET A   978
REMARK 465     ASP A   979
REMARK 465     GLU A   980
REMARK 465     GLU A   981
REMARK 465     ASP A   982
REMARK 465     MET A   983
REMARK 465     ASP A   984
REMARK 465     ASP A   985
REMARK 465     VAL A   986
REMARK 465     VAL A   987
REMARK 465     ASP A   988
REMARK 465     ALA A   989
REMARK 465     ASP A   990
REMARK 465     GLU A   991
REMARK 465     TYR A   992
REMARK 465     LEU A   993
REMARK 465     ILE A   994
REMARK 465     PRO A   995
REMARK 465     GLN A   996
REMARK 465     GLN A   997
REMARK 465     GLY A   998
REMARK 465     GLY B   669
REMARK 465     ALA B   670
REMARK 465     MET B   671
REMARK 465     GLY B   672
REMARK 465     GLU B   673
REMARK 465     ALA B   674
REMARK 465     PRO B   675
REMARK 465     ASN B   676
REMARK 465     GLY B   711
REMARK 465     GLU B   712
REMARK 465     LYS B   713
REMARK 465     VAL B   714
REMARK 465     GLU B   725
REMARK 465     ALA B   726
REMARK 465     THR B   727
REMARK 465     SER B   728
REMARK 465     PRO B   729
REMARK 465     LYS B   730
REMARK 465     ALA B   840
REMARK 465     GLU B   841
REMARK 465     GLU B   842
REMARK 465     LYS B   843
REMARK 465     GLU B   848
REMARK 465     GLY B   849
REMARK 465     ARG B   962
REMARK 465     MET B   963
REMARK 465     HIS B   964
REMARK 465     LEU B   965
REMARK 465     PRO B   966
REMARK 465     SER B   967
REMARK 465     PRO B   968
REMARK 465     THR B   969
REMARK 465     ASP B   970
REMARK 465     SER B   971
REMARK 465     ASN B   972
REMARK 465     PHE B   973
REMARK 465     TYR B   974
REMARK 465     ARG B   975
REMARK 465     ALA B   976
REMARK 465     LEU B   977
REMARK 465     MET B   978
REMARK 465     ASP B   979
REMARK 465     GLU B   980
REMARK 465     GLU B   981
REMARK 465     ASP B   982
REMARK 465     MET B   983
REMARK 465     ASP B   984
REMARK 465     ASP B   985
REMARK 465     VAL B   986
REMARK 465     VAL B   987
REMARK 465     ASP B   988
REMARK 465     ALA B   989
REMARK 465     ASP B   990
REMARK 465     GLU B   991
REMARK 465     TYR B   992
REMARK 465     LEU B   993
REMARK 465     ILE B   994
REMARK 465     PRO B   995
REMARK 465     GLN B   996
REMARK 465     GLN B   997
REMARK 465     GLY B   998
REMARK 465     GLY C   310
REMARK 465     PRO C   311
REMARK 465     LEU C   312
REMARK 465     GLY C   313
REMARK 465     SER C   314
REMARK 465     ARG C   315
REMARK 465     PRO C   316
REMARK 465     PRO C   317
REMARK 465     LYS C   318
REMARK 465     VAL C   319
REMARK 465     PRO C   320
REMARK 465     PRO C   321
REMARK 465     ARG C   322
REMARK 465     GLU C   323
REMARK 465     PRO C   324
REMARK 465     LEU C   325
REMARK 465     SER C   326
REMARK 465     PRO C   327
REMARK 465     SER C   328
REMARK 465     ASN C   329
REMARK 465     SER C   330
REMARK 465     ARG C   331
REMARK 465     THR C   332
REMARK 465     PRO C   333
REMARK 465     SER C   334
REMARK 465     PRO C   335
REMARK 465     ALA C   363
REMARK 465     LEU C   364
REMARK 465     GLN C   365
REMARK 465     ARG C   366
REMARK 465     GLN C   367
REMARK 465     ASN C   368
REMARK 465     SER C   369
REMARK 465     GLU C   370
REMARK 465     GLY C   371
REMARK 465     SER C   372
REMARK 465     ALA C   373
REMARK 465     SER C   374
REMARK 465     GLY D   310
REMARK 465     PRO D   311
REMARK 465     LEU D   312
REMARK 465     GLY D   313
REMARK 465     SER D   314
REMARK 465     ARG D   315
REMARK 465     PRO D   316
REMARK 465     PRO D   317
REMARK 465     LYS D   318
REMARK 465     VAL D   319
REMARK 465     PRO D   320
REMARK 465     PRO D   321
REMARK 465     ARG D   322
REMARK 465     GLU D   323
REMARK 465     PRO D   324
REMARK 465     LEU D   325
REMARK 465     SER D   326
REMARK 465     PRO D   327
REMARK 465     SER D   328
REMARK 465     ASN D   329
REMARK 465     SER D   330
REMARK 465     ARG D   331
REMARK 465     THR D   332
REMARK 465     PRO D   333
REMARK 465     SER D   334
REMARK 465     PRO D   335
REMARK 465     LYS D   336
REMARK 465     ALA D   363
REMARK 465     LEU D   364
REMARK 465     GLN D   365
REMARK 465     ARG D   366
REMARK 465     GLN D   367
REMARK 465     ASN D   368
REMARK 465     SER D   369
REMARK 465     GLU D   370
REMARK 465     GLY D   371
REMARK 465     SER D   372
REMARK 465     ALA D   373
REMARK 465     SER D   374
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     GLN A 677    CG   CD   OE1  NE2
REMARK 470     LEU A 680    CG   CD1  CD2
REMARK 470     ARG A 681    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 684    CG   CD   CE   NZ
REMARK 470     LYS A 689    CG   CD   CE   NZ
REMARK 470     LYS A 690    CG   CD   CE   NZ
REMARK 470     LYS A 692    CG   CD   CE   NZ
REMARK 470     LEU A 694    CG   CD1  CD2
REMARK 470     PHE A 699    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 704    CG   CD   CE   NZ
REMARK 470     LEU A 706    CG   CD1  CD2
REMARK 470     GLU A 710    CG   CD   OE1  OE2
REMARK 470     LYS A 713    CG   CD   CE   NZ
REMARK 470     VAL A 714    CG1  CG2
REMARK 470     LYS A 715    CG   CD   CE   NZ
REMARK 470     GLU A 725    CG   CD   OE1  OE2
REMARK 470     PRO A 729    CG   CD
REMARK 470     LYS A 730    CG   CD   CE   NZ
REMARK 470     ASN A 732    CG   OD1  ND2
REMARK 470     GLU A 738    CG   CD   OE1  OE2
REMARK 470     TYR A 740    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     ARG A 752    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU A 754    CG   CD1  CD2
REMARK 470     GLU A 780    CG   CD   OE1  OE2
REMARK 470     LYS A 782    CG   CD   CE   NZ
REMARK 470     ASP A 783    CG   OD1  OD2
REMARK 470     ARG A 807    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A 808    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 822    CG   CD   CE   NZ
REMARK 470     GLN A 825    CG   CD   OE1  NE2
REMARK 470     LYS A 836    CG   CD   CE   NZ
REMARK 470     LEU A 837    CG   CD1  CD2
REMARK 470     GLU A 841    CG   CD   OE1  OE2
REMARK 470     GLU A 842    CG   CD   OE1  OE2
REMARK 470     LYS A 843    CG   CD   CE   NZ
REMARK 470     GLU A 844    CG   CD   OE1  OE2
REMARK 470     LYS A 889    CG   CD   CE   NZ
REMARK 470     LYS A 905    CG   CD   CE   NZ
REMARK 470     ARG A 938    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU A 943    CG   CD   OE1  OE2
REMARK 470     ARG A 949    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASP A 950    CG   OD1  OD2
REMARK 470     GLN A 952    CG   CD   OE1  NE2
REMARK 470     GLN A 958    CG   CD   OE1  NE2
REMARK 470     GLN B 677    CG   CD   OE1  NE2
REMARK 470     LEU B 679    CG   CD1  CD2
REMARK 470     LEU B 680    CG   CD1  CD2
REMARK 470     ARG B 681    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU B 683    CG   CD1  CD2
REMARK 470     LYS B 684    CG   CD   CE   NZ
REMARK 470     LYS B 689    CG   CD   CE   NZ
REMARK 470     LYS B 692    CG   CD   CE   NZ
REMARK 470     LEU B 694    CG   CD1  CD2
REMARK 470     LYS B 704    CG   CD   CE   NZ
REMARK 470     LEU B 706    CG   CD1  CD2
REMARK 470     ILE B 708    CG1  CG2  CD1
REMARK 470     LYS B 715    CG   CD   CE   NZ
REMARK 470     ASN B 732    CG   OD1  ND2
REMARK 470     LYS B 733    CG   CD   CE   NZ
REMARK 470     ASP B 737    CG   OD1  OD2
REMARK 470     GLU B 738    CG   CD   OE1  OE2
REMARK 470     TYR B 740    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     LEU B 753    CG   CD1  CD2
REMARK 470     LEU B 754    CG   CD1  CD2
REMARK 470     GLN B 767    CG   CD   OE1  NE2
REMARK 470     GLU B 780    CG   CD   OE1  OE2
REMARK 470     LYS B 782    CG   CD   CE   NZ
REMARK 470     LEU B 791    CG   CD1  CD2
REMARK 470     ARG B 807    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 822    CG   CD   CE   NZ
REMARK 470     GLU B 844    CG   CD   OE1  OE2
REMARK 470     LYS B 851    CG   CD   CE   NZ
REMARK 470     ARG B 865    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU B 898    CG   CD   OE1  OE2
REMARK 470     LYS B 905    CG   CD   CE   NZ
REMARK 470     ARG B 938    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 946    CG   CD   CE   NZ
REMARK 470     ARG B 949    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN B 952    CG   CD   OE1  NE2
REMARK 470     ARG B 953    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASP B 960    CG   OD1  OD2
REMARK 470     GLU B 961    CG   CD   OE1  OE2
REMARK 470     LYS C 336    CG   CD   CE   NZ
REMARK 470     SER C 340    OG
REMARK 470     LEU C 342    CG   CD1  CD2
REMARK 470     ASN C 343    CG   OD1  ND2
REMARK 470     GLN C 350    CG   CD   OE1  NE2
REMARK 470     LYS C 357    CG   CD   CE   NZ
REMARK 470     LYS C 362    CG   CD   CE   NZ
REMARK 470     SER D 340    OG
REMARK 470     LEU D 342    CG   CD1  CD2
REMARK 470     ASN D 343    CG   OD1  ND2
REMARK 470     VAL D 345    CG1  CG2
REMARK 470     THR D 349    OG1  CG2
REMARK 470     GLN D 350    CG   CD   OE1  NE2
REMARK 470     LYS D 357    CG   CD   CE   NZ
REMARK 470     LYS D 362    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    GLY A   839     N    GLU A   841              2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ASN A 676     -166.21     51.07
REMARK 500    GLN A 677       31.70    -98.50
REMARK 500    LEU A 679      121.29     69.66
REMARK 500    LEU A 680       69.14     75.77
REMARK 500    GLU A 685       59.63    -62.69
REMARK 500    THR A 686       -2.64   -159.13
REMARK 500    PHE A 688      137.40   -178.25
REMARK 500    ILE A 691      -91.68    -96.65
REMARK 500    TYR A 703     -152.95   -121.34
REMARK 500    LYS A 704       84.20   -160.22
REMARK 500    PRO A 709       99.65    -49.89
REMARK 500    GLU A 710      118.07    -17.23
REMARK 500    GLU A 712       90.74    -21.15
REMARK 500    LYS A 713       -1.22    -44.62
REMARK 500    LYS A 730       18.04    -56.07
REMARK 500    GLU A 734      -70.52    -69.03
REMARK 500    ILE A 735      -57.08    -26.68
REMARK 500    MET A 742       -1.30    -54.97
REMARK 500    SER A 744       38.90    -67.81
REMARK 500    HIS A 749       29.90   -142.93
REMARK 500    CYS A 751       78.11    -37.05
REMARK 500    ARG A 752      133.38    -35.34
REMARK 500    THR A 759     -136.83   -116.33
REMARK 500    THR A 761      113.82   -171.49
REMARK 500    GLN A 767       95.80    -55.16
REMARK 500    PRO A 770      -60.95    -91.86
REMARK 500    LEU A 774      -16.47    -49.28
REMARK 500    ASP A 783       45.30    -82.02
REMARK 500    ASN A 784      -23.14   -158.72
REMARK 500    GLN A 788      -86.49    -24.06
REMARK 500    ASN A 792      -79.81    -56.36
REMARK 500    TRP A 793      -56.36    -22.08
REMARK 500    ARG A 807       52.45   -146.59
REMARK 500    ARG A 808       46.22     28.23
REMARK 500    ARG A 812      -56.62     81.96
REMARK 500    LYS A 822      -75.68    -71.01
REMARK 500    ALA A 835     -149.94    -60.55
REMARK 500    LYS A 836      135.51    166.78
REMARK 500    ALA A 840      -45.09     18.83
REMARK 500    LYS A 851      -17.42    170.52
REMARK 500    VAL A 852      109.88     56.97
REMARK 500    LYS A 855      -18.55    -45.77
REMARK 500    ALA A 858     -170.66    -60.86
REMARK 500    ARG A 865       50.62     30.23
REMARK 500    GLU A 882      -72.89    -42.40
REMARK 500    PHE A 886       63.01     60.26
REMARK 500    TYR A 891      -20.08     76.82
REMARK 500    ASP A 892      111.29    -13.15
REMARK 500    PRO A 895      148.60    -28.07
REMARK 500    SER A 901      -34.05    -37.02
REMARK 500    LYS A 905        7.68    -66.87
REMARK 500    PRO A 910      175.22    -59.84
REMARK 500    ILE A 917        7.34    -61.65
REMARK 500    ASP A 932       43.17    -98.99
REMARK 500    LYS A 946      -68.01   -100.66
REMARK 500    ARG A 949       -5.68    -57.36
REMARK 500    ASP A 950       53.85   -160.79
REMARK 500    GLN A 952      -18.59    -48.59
REMARK 500    ALA B 678        2.13    171.43
REMARK 500    LEU B 679      -20.07    173.20
REMARK 500    LEU B 680      173.28    -53.11
REMARK 500    GLU B 685       13.47    -65.65
REMARK 500    GLU B 687       60.29    -65.29
REMARK 500    PHE B 688      152.82    163.34
REMARK 500    ILE B 691     -115.94   -103.48
REMARK 500    LEU B 723     -165.58   -104.98
REMARK 500    ASN B 732       31.55    -59.57
REMARK 500    MET B 742       -6.67    -57.72
REMARK 500    ASN B 747      134.85   -170.44
REMARK 500    VAL B 750      119.78   -161.89
REMARK 500    LEU B 754      -92.09    -80.51
REMARK 500    THR B 759     -137.50   -146.10
REMARK 500    GLN B 767       70.20    -54.79
REMARK 500    LEU B 768      125.92    -18.39
REMARK 500    ASN B 784      -43.32   -158.14
REMARK 500    ARG B 808       29.02     44.83
REMARK 500    ARG B 812      -11.36     73.77
REMARK 500    ASP B 813       61.17   -154.74
REMARK 500    ALA B 815      156.63    163.98
REMARK 500    PHE B 832       36.83   -159.16
REMARK 500    LYS B 855       -4.74    -51.39
REMARK 500    GLU B 860       -9.49    -54.17
REMARK 500    VAL B 873      -71.08    -26.26
REMARK 500    MET B 884      -70.41    -56.94
REMARK 500    THR B 885        0.08    -56.55
REMARK 500    PHE B 886       62.61     60.53
REMARK 500    TYR B 891       -0.03     65.19
REMARK 500    ASP B 892      146.12    -24.99
REMARK 500    PRO B 913      -12.72    -45.30
REMARK 500    TRP B 927       36.91    -94.06
REMARK 500    ARG B 934      166.40    -46.72
REMARK 500    ARG B 949      -33.13    -38.07
REMARK 500    GLN B 952      -35.73    -39.96
REMARK 500    ILE B 957     -158.41   -136.27
REMARK 500    ASP B 960       37.77    -70.19
REMARK 500    SER C 337       74.98   -150.27
REMARK 500    ASN C 343       40.67     98.16
REMARK 500    VAL C 345       99.48    -63.74
REMARK 500    SER C 361       90.55    -68.54
REMARK 500    LEU D 342       46.33    -92.22
REMARK 500    ASN D 343      101.60     72.17
REMARK 500    VAL D 345       90.23     -8.58
REMARK 500    PRO D 347      143.07    -39.13
REMARK 500    ASP D 355      107.95    -43.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    TYR A 891         0.07    SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2RFD   RELATED DB: PDB
REMARK 900 RELATED ID: 2RFE   RELATED DB: PDB
DBREF  2RF9 A  672   998  UNP    P00533   EGFR_HUMAN     696   1022
DBREF  2RF9 B  672   998  UNP    P00533   EGFR_HUMAN     696   1022
DBREF  2RF9 C  315   374  UNP    Q9UJM3   ERRFI_HUMAN    315    374
DBREF  2RF9 D  315   374  UNP    Q9UJM3   ERRFI_HUMAN    315    374
SEQADV 2RF9 GLY A  669  UNP  P00533              EXPRESSION TAG
SEQADV 2RF9 ALA A  670  UNP  P00533              EXPRESSION TAG
SEQADV 2RF9 MET A  671  UNP  P00533              EXPRESSION TAG
SEQADV 2RF9 GLY B  669  UNP  P00533              EXPRESSION TAG
SEQADV 2RF9 ALA B  670  UNP  P00533              EXPRESSION TAG
SEQADV 2RF9 MET B  671  UNP  P00533              EXPRESSION TAG
SEQADV 2RF9 GLY C  310  UNP  Q9UJM3              EXPRESSION TAG
SEQADV 2RF9 PRO C  311  UNP  Q9UJM3              EXPRESSION TAG
SEQADV 2RF9 LEU C  312  UNP  Q9UJM3              EXPRESSION TAG
SEQADV 2RF9 GLY C  313  UNP  Q9UJM3              EXPRESSION TAG
SEQADV 2RF9 SER C  314  UNP  Q9UJM3              EXPRESSION TAG
SEQADV 2RF9 GLY D  310  UNP  Q9UJM3              EXPRESSION TAG
SEQADV 2RF9 PRO D  311  UNP  Q9UJM3              EXPRESSION TAG
SEQADV 2RF9 LEU D  312  UNP  Q9UJM3              EXPRESSION TAG
SEQADV 2RF9 GLY D  313  UNP  Q9UJM3              EXPRESSION TAG
SEQADV 2RF9 SER D  314  UNP  Q9UJM3              EXPRESSION TAG
SEQRES   1 A  330  GLY ALA MET GLY GLU ALA PRO ASN GLN ALA LEU LEU ARG
SEQRES   2 A  330  ILE LEU LYS GLU THR GLU PHE LYS LYS ILE LYS VAL LEU
SEQRES   3 A  330  GLY SER GLY ALA PHE GLY THR VAL TYR LYS GLY LEU TRP
SEQRES   4 A  330  ILE PRO GLU GLY GLU LYS VAL LYS ILE PRO VAL ALA ILE
SEQRES   5 A  330  LYS GLU LEU ARG GLU ALA THR SER PRO LYS ALA ASN LYS
SEQRES   6 A  330  GLU ILE LEU ASP GLU ALA TYR VAL MET ALA SER VAL ASP
SEQRES   7 A  330  ASN PRO HIS VAL CYS ARG LEU LEU GLY ILE CYS LEU THR
SEQRES   8 A  330  SER THR VAL GLN LEU ILE THR GLN LEU MET PRO PHE GLY
SEQRES   9 A  330  CYS LEU LEU ASP TYR VAL ARG GLU HIS LYS ASP ASN ILE
SEQRES  10 A  330  GLY SER GLN TYR LEU LEU ASN TRP CYS VAL GLN ILE ALA
SEQRES  11 A  330  LYS GLY MET ASN TYR LEU GLU ASP ARG ARG LEU VAL HIS
SEQRES  12 A  330  ARG ASP LEU ALA ALA ARG ASN VAL LEU VAL LYS THR PRO
SEQRES  13 A  330  GLN HIS VAL LYS ILE THR ASP PHE GLY LEU ALA LYS LEU
SEQRES  14 A  330  LEU GLY ALA GLU GLU LYS GLU TYR HIS ALA GLU GLY GLY
SEQRES  15 A  330  LYS VAL PRO ILE LYS TRP MET ALA LEU GLU SER ILE LEU
SEQRES  16 A  330  HIS ARG ILE TYR THR HIS GLN SER ASP VAL TRP SER TYR
SEQRES  17 A  330  GLY VAL THR VAL TRP GLU LEU MET THR PHE GLY SER LYS
SEQRES  18 A  330  PRO TYR ASP GLY ILE PRO ALA SER GLU ILE SER SER ILE
SEQRES  19 A  330  LEU GLU LYS GLY GLU ARG LEU PRO GLN PRO PRO ILE CYS
SEQRES  20 A  330  THR ILE ASP VAL TYR MET ILE MET VAL LYS CYS TRP MET
SEQRES  21 A  330  ILE ASP ALA ASP SER ARG PRO LYS PHE ARG GLU LEU ILE
SEQRES  22 A  330  ILE GLU PHE SER LYS MET ALA ARG ASP PRO GLN ARG TYR
SEQRES  23 A  330  LEU VAL ILE GLN GLY ASP GLU ARG MET HIS LEU PRO SER
SEQRES  24 A  330  PRO THR ASP SER ASN PHE TYR ARG ALA LEU MET ASP GLU
SEQRES  25 A  330  GLU ASP MET ASP ASP VAL VAL ASP ALA ASP GLU TYR LEU
SEQRES  26 A  330  ILE PRO GLN GLN GLY
SEQRES   1 B  330  GLY ALA MET GLY GLU ALA PRO ASN GLN ALA LEU LEU ARG
SEQRES   2 B  330  ILE LEU LYS GLU THR GLU PHE LYS LYS ILE LYS VAL LEU
SEQRES   3 B  330  GLY SER GLY ALA PHE GLY THR VAL TYR LYS GLY LEU TRP
SEQRES   4 B  330  ILE PRO GLU GLY GLU LYS VAL LYS ILE PRO VAL ALA ILE
SEQRES   5 B  330  LYS GLU LEU ARG GLU ALA THR SER PRO LYS ALA ASN LYS
SEQRES   6 B  330  GLU ILE LEU ASP GLU ALA TYR VAL MET ALA SER VAL ASP
SEQRES   7 B  330  ASN PRO HIS VAL CYS ARG LEU LEU GLY ILE CYS LEU THR
SEQRES   8 B  330  SER THR VAL GLN LEU ILE THR GLN LEU MET PRO PHE GLY
SEQRES   9 B  330  CYS LEU LEU ASP TYR VAL ARG GLU HIS LYS ASP ASN ILE
SEQRES  10 B  330  GLY SER GLN TYR LEU LEU ASN TRP CYS VAL GLN ILE ALA
SEQRES  11 B  330  LYS GLY MET ASN TYR LEU GLU ASP ARG ARG LEU VAL HIS
SEQRES  12 B  330  ARG ASP LEU ALA ALA ARG ASN VAL LEU VAL LYS THR PRO
SEQRES  13 B  330  GLN HIS VAL LYS ILE THR ASP PHE GLY LEU ALA LYS LEU
SEQRES  14 B  330  LEU GLY ALA GLU GLU LYS GLU TYR HIS ALA GLU GLY GLY
SEQRES  15 B  330  LYS VAL PRO ILE LYS TRP MET ALA LEU GLU SER ILE LEU
SEQRES  16 B  330  HIS ARG ILE TYR THR HIS GLN SER ASP VAL TRP SER TYR
SEQRES  17 B  330  GLY VAL THR VAL TRP GLU LEU MET THR PHE GLY SER LYS
SEQRES  18 B  330  PRO TYR ASP GLY ILE PRO ALA SER GLU ILE SER SER ILE
SEQRES  19 B  330  LEU GLU LYS GLY GLU ARG LEU PRO GLN PRO PRO ILE CYS
SEQRES  20 B  330  THR ILE ASP VAL TYR MET ILE MET VAL LYS CYS TRP MET
SEQRES  21 B  330  ILE ASP ALA ASP SER ARG PRO LYS PHE ARG GLU LEU ILE
SEQRES  22 B  330  ILE GLU PHE SER LYS MET ALA ARG ASP PRO GLN ARG TYR
SEQRES  23 B  330  LEU VAL ILE GLN GLY ASP GLU ARG MET HIS LEU PRO SER
SEQRES  24 B  330  PRO THR ASP SER ASN PHE TYR ARG ALA LEU MET ASP GLU
SEQRES  25 B  330  GLU ASP MET ASP ASP VAL VAL ASP ALA ASP GLU TYR LEU
SEQRES  26 B  330  ILE PRO GLN GLN GLY
SEQRES   1 C   65  GLY PRO LEU GLY SER ARG PRO PRO LYS VAL PRO PRO ARG
SEQRES   2 C   65  GLU PRO LEU SER PRO SER ASN SER ARG THR PRO SER PRO
SEQRES   3 C   65  LYS SER LEU PRO SER TYR LEU ASN GLY VAL MET PRO PRO
SEQRES   4 C   65  THR GLN SER PHE ALA PRO ASP PRO LYS TYR VAL SER SER
SEQRES   5 C   65  LYS ALA LEU GLN ARG GLN ASN SER GLU GLY SER ALA SER
SEQRES   1 D   65  GLY PRO LEU GLY SER ARG PRO PRO LYS VAL PRO PRO ARG
SEQRES   2 D   65  GLU PRO LEU SER PRO SER ASN SER ARG THR PRO SER PRO
SEQRES   3 D   65  LYS SER LEU PRO SER TYR LEU ASN GLY VAL MET PRO PRO
SEQRES   4 D   65  THR GLN SER PHE ALA PRO ASP PRO LYS TYR VAL SER SER
SEQRES   5 D   65  LYS ALA LEU GLN ARG GLN ASN SER GLU GLY SER ALA SER
HELIX    1   1 ALA A  731  ALA A  743  1                                  13
HELIX    2   2 CYS A  773  HIS A  781  1                                   9
HELIX    3   3 LYS A  782  ILE A  785  5                                   4
HELIX    4   4 GLY A  786  ASP A  806  1                                  21
HELIX    5   5 PRO A  853  MET A  857  5                                   5
HELIX    6   6 ALA A  858  LEU A  863  1                                   6
HELIX    7   7 THR A  868  THR A  885  1                                  18
HELIX    8   8 SER A  897  GLU A  904  1                                   8
HELIX    9   9 VAL A  919  TRP A  927  1                                   9
HELIX   10  10 ASP A  930  ARG A  934  5                                   5
HELIX   11  11 LYS A  936  ALA A  948  1                                  13
HELIX   12  12 ASP A  950  LEU A  955  1                                   6
HELIX   13  13 ASN B  732  SER B  744  1                                  13
HELIX   14  14 CYS B  773  HIS B  781  1                                   9
HELIX   15  15 GLY B  786  ASP B  806  1                                  21
HELIX   16  16 ALA B  858  LEU B  863  1                                   6
HELIX   17  17 THR B  868  THR B  885  1                                  18
HELIX   18  18 GLU B  898  GLU B  904  1                                   7
HELIX   19  19 THR B  916  TRP B  927  1                                  12
HELIX   20  20 LYS B  936  ASP B  950  1                                  15
SHEET    1   A 3 ARG A 681  LEU A 683  0
SHEET    2   A 3 LEU A 753  LEU A 758  1  O  ILE A 756   N  LEU A 683
SHEET    3   A 3 VAL A 762  THR A 766 -1  O  GLN A 763   N  CYS A 757
SHEET    1   B 3 LYS A 689  GLY A 697  0
SHEET    2   B 3 GLY A 700  TRP A 707 -1  O  GLY A 700   N  GLY A 697
SHEET    3   B 3 ILE A 716  PRO A 717 -1  O  ILE A 716   N  TRP A 707
SHEET    1   C 2 VAL A 819  THR A 823  0
SHEET    2   C 2 HIS A 826  ILE A 829 -1  O  HIS A 826   N  THR A 823
SHEET    1   D 2 TYR A 845  HIS A 846  0
SHEET    2   D 2 ILE A 866  TYR A 867 -1  O  TYR A 867   N  TYR A 845
SHEET    1   E 2 GLU A 907  ARG A 908  0
SHEET    2   E 2 GLN C 350  SER C 351 -1  O  GLN C 350   N  ARG A 908
SHEET    1   F 3 LYS B 689  GLY B 695  0
SHEET    2   F 3 GLY B 700  TRP B 707 -1  O  LYS B 704   N  LYS B 692
SHEET    3   F 3 ILE B 716  LEU B 723 -1  O  ILE B 720   N  TYR B 703
SHEET    1   G 2 ILE B 756  CYS B 757  0
SHEET    2   G 2 GLN B 763  LEU B 764 -1  O  GLN B 763   N  CYS B 757
SHEET    1   H 2 LEU B 809  VAL B 810  0
SHEET    2   H 2 LYS B 836  LEU B 837 -1  O  LYS B 836   N  VAL B 810
SHEET    1   I 2 VAL B 819  THR B 823  0
SHEET    2   I 2 HIS B 826  ILE B 829 -1  O  LYS B 828   N  LEU B 820
SHEET    1   J 2 GLU B 907  ARG B 908  0
SHEET    2   J 2 GLN D 350  SER D 351 -1  O  GLN D 350   N  ARG B 908
CISPEP   1 ALA C  353    PRO C  354          0         0.89
CISPEP   2 ALA D  353    PRO D  354          0         1.59
CRYST1  188.762   42.650   99.726  90.00 109.12  90.00 C 1 2 1       8
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.005298  0.000000  0.001837        0.00000
SCALE2      0.000000  0.023447  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010613        0.00000
      
PROCHECK
Go to PROCHECK summary
 References